A Fluorescence-Based Supramolecular Tandem Assay for Monitoring Lysine Methyltransferase Activity in Homogeneous Solution (Q57267592)

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24 January 2020

title

A fluorescence-based supramolecular tandem assay for monitoring lysine methyltransferase activity in homogeneous solution (English)

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histone-lysine N-methyltransferase

24 January 2020

main subject

general chemistry

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author

Albert Jeltsch

5

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24 January 2020

Werner M Nau

6

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24 January 2020

author name string

Mara Florea

1

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24 January 2020

Srikanth Kudithipudi

2

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24 January 2020

Ana Rei

3

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24 January 2020

María José González-Álvarez

4

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24 January 2020

language of work or name

English

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publication date

24 February 2012

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Chemistry—A European Journal

24 January 2020

published in

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24 January 2020

volume

18

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24 January 2020

issue

12

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24 January 2020

page(s)

3521-3528

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Methylation of histone H3 at lysine 4 is highly conserved and correlates with transcriptionally active nuclei in Tetrahymena

24 January 2020

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Adding a Lysine Mimic in the Design of Potent Inhibitors of Histone Lysine Methyltransferases

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The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity

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Continuous enzymatic assay for histone lysine methyltransferases

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Partitioning and plasticity of repressive histone methylation states in mammalian chromatin

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Identifiers

DOI

10.1002/CHEM.201103397

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22367964%20AND%20SRC:MED&resulttype=core&format=json

24 January 2020

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